Noncovalent interaction between amyloid-beta-peptide (1-40) and oleuropein studied by electrospray ionization mass spectrometry

Journal of the American Society for Mass Spectrometry
Fotini N BazotiAnthony Tsarbopoulos

Abstract

Beta amyloid peptide (Abeta) is the major proteinaceous component of senile plaques formed in Alzheimer's disease (AD) brain. The aggregation of Abeta is associated with neurodegeneration, loss of cognitive ability, and premature death. It has been suggested that oxidative stress and generation of free radical species have implications in the fibrillation of Abeta and its subsequent neurotoxicity. For this reason, it is proposed that antioxidants may offer a protective or therapeutic alternative against amyloidosis. This study is the first report of the formation of the noncovalent complex between Abeta or its oxidized form and the natural derived antioxidant oleuropein (OE) by electrospray ionization mass spectrometry (ESI MS). ESI MS allowed the real time monitoring of the complex formation between Abeta, OE, and variants thereof. Several experimental conditions, such as elevated orifice potential, low pH values, presence of organic modifier, and ligand concentration were examined, to assess the specificity and the stability of the formed noncovalent complexes.

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Citations

May 2, 2008·Journal of the American Society for Mass Spectrometry·Fotini N BazotiAnthony Tsarbopoulos
Jan 25, 2008·Acta Pharmacologica Sinica·Hong-fang Ji, Hong-yu Zhang
Feb 1, 2014·Journal of Agricultural and Food Chemistry·Ting HuXi-Lin Xu
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Oct 25, 2020·Scientific Reports·Nikolaos Stavros KoulakiotisAnthony Tsarbopoulos
Jun 3, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Ioana Cezara CabaBogdan Ionel Tamba
May 18, 2019·Journal of the American Society for Mass Spectrometry·Yun ShenZhixin Tian

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